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Database: UniProt
Entry: S6CEQ1_9GAMM
LinkDB: S6CEQ1_9GAMM
Original site: S6CEQ1_9GAMM 
ID   S6CEQ1_9GAMM            Unreviewed;       457 AA.
AC   S6CEQ1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=M16 family peptidase {ECO:0000313|EMBL:BAN68255.1};
DE            EC=3.4.24.64 {ECO:0000313|EMBL:BAN68255.1};
GN   ORFNames=EBS_0272 {ECO:0000313|EMBL:BAN68255.1};
OS   endosymbiont of unidentified scaly snail isolate Monju.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN68255.1, ECO:0000313|Proteomes:UP000015562};
RN   [1] {ECO:0000313|EMBL:BAN68255.1, ECO:0000313|Proteomes:UP000015562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Monju {ECO:0000313|EMBL:BAN68255.1};
RX   PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA   Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA   Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA   Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT   "Allying with armored snails: the complete genome of gammaproteobacterial
RT   endosymbiont.";
RL   ISME J. 8:40-51(2014).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; AP012978; BAN68255.1; -; Genomic_DNA.
DR   RefSeq; WP_043106971.1; NZ_AP012978.1.
DR   AlphaFoldDB; S6CEQ1; -.
DR   STRING; 1248727.EBS_0272; -.
DR   MEROPS; M16.019; -.
DR   KEGG; enm:EBS_0272; -.
DR   HOGENOM; CLU_009902_1_0_6; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000015562; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAN68255.1};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015562};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..457
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004547255"
FT   DOMAIN          35..180
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          190..370
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   457 AA;  51056 MW;  1C1BEF3B591CD5F2 CRC64;
     MFSRLLSVLL ALLPAIAAAG AAPVHEFLLD NGLKVIVKEE HRAPVAVSQV WYRIGSSYEE
     GGRTGLSHLL EHMMFKGTRA HGPGEFSRIV AELGGSENAF TSRDYTAYFE TLSVEHLDRA
     LELEADRMRN VVFEEKEFRK ELAVVMEERR MRTDDSPSGL TYEQLMAVAW RASPYQNPVI
     GWMDDLANME IDALQRWYDF WYQPNNATLV VVGDVDPQQV LALAKKHFGP IPAGKVPAPR
     RPAEPEQRGI TRVTVKAPAK QPYVLMGYKV PNLASAEHDW EPYALTVAAA VLDGGASARL
     ARDLVRGRKI AASAGAQYDL YSRLPGLFLF DGTPTEGHRA AEVEQALREE VKRLQETLVS
     REELDRVVTQ AVAAKVFQAD SIFYQAMEIG ILETIGLDWH LLEREIERLR AVTPEQVQAV
     ARKYLKDDYL TVATLVPQPT DKPVRTTPIT RGTTHGK
//
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